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Volumn 22, Issue 2, 2012, Pages 250-262

Targeted Disruption of Heparan Sulfate Interaction with Hepatocyte and Vascular Endothelial Growth Factors Blocks Normal and Oncogenic Signaling

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; HEPARAN SULFATE; NK1 3S PROTEIN; SCATTER FACTOR; UNCLASSIFIED DRUG; VASCULOTROPIN;

EID: 84865107470     PISSN: 15356108     EISSN: 18783686     Source Type: Journal    
DOI: 10.1016/j.ccr.2012.06.029     Document Type: Article
Times cited : (40)

References (51)
  • 3
    • 33746504571 scopus 로고    scopus 로고
    • Invasive growth: a MET-driven genetic programme for cancer and stem cells
    • Boccaccio C., Comoglio P.M. Invasive growth: a MET-driven genetic programme for cancer and stem cells. Nat. Rev. Cancer 2006, 6:637-645.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 637-645
    • Boccaccio, C.1    Comoglio, P.M.2
  • 6
    • 77950552463 scopus 로고    scopus 로고
    • Targeting the HGF/Met signalling pathway in cancer
    • Cecchi F., Rabe D.C., Bottaro D.P. Targeting the HGF/Met signalling pathway in cancer. Eur. J. Cancer 2010, 46:1260-1270.
    • (2010) Eur. J. Cancer , vol.46 , pp. 1260-1270
    • Cecchi, F.1    Rabe, D.C.2    Bottaro, D.P.3
  • 7
    • 0032957467 scopus 로고    scopus 로고
    • Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding
    • Chirgadze D.Y., Hepple J.P., Zhou H., Byrd R.A., Blundell T.L., Gherardi E. Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding. Nat. Struct. Biol. 1999, 6:72-79.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 72-79
    • Chirgadze, D.Y.1    Hepple, J.P.2    Zhou, H.3    Byrd, R.A.4    Blundell, T.L.5    Gherardi, E.6
  • 8
    • 1642297115 scopus 로고    scopus 로고
    • The crystal structure of placental growth factor in complex with domain 2 of vascular endothelial growth factor receptor-1
    • Christinger H.W., Fuh G., de Vos A.M., Wiesmann C. The crystal structure of placental growth factor in complex with domain 2 of vascular endothelial growth factor receptor-1. J. Biol. Chem. 2004, 279:10382-10388.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10382-10388
    • Christinger, H.W.1    Fuh, G.2    de Vos, A.M.3    Wiesmann, C.4
  • 11
    • 4143136640 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: basic science and clinical progress
    • Ferrara N. Vascular endothelial growth factor: basic science and clinical progress. Endocr. Rev. 2004, 25:581-611.
    • (2004) Endocr. Rev. , vol.25 , pp. 581-611
    • Ferrara, N.1
  • 12
    • 0032080310 scopus 로고    scopus 로고
    • Requirements for binding and signaling of the kinase domain receptor for vascular endothelial growth factor
    • Fuh G., Li B., Crowley C., Cunningham B., Wells J.A. Requirements for binding and signaling of the kinase domain receptor for vascular endothelial growth factor. J. Biol. Chem. 1998, 273:11197-11204.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11197-11204
    • Fuh, G.1    Li, B.2    Crowley, C.3    Cunningham, B.4    Wells, J.A.5
  • 13
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: glycans as novel therapeutic targets
    • Fuster M.M., Esko J.D. The sweet and sour of cancer: glycans as novel therapeutic targets. Nat. Rev. Cancer 2005, 5:526-542.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 16
    • 0034674108 scopus 로고    scopus 로고
    • Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165 [corrected]
    • Gluzman-Poltorak Z., Cohen T., Herzog Y., Neufeld G. Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165 [corrected]. J. Biol. Chem. 2000, 275:18040-18045.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18040-18045
    • Gluzman-Poltorak, Z.1    Cohen, T.2    Herzog, Y.3    Neufeld, G.4
  • 18
    • 0032560080 scopus 로고    scopus 로고
    • Identification of heparin-binding stretches of a naturally occurring deleted variant of hepatocyte growth factor (dHGF)
    • Kinosaki M., Yamaguchi K., Murakami A., Ueda M., Morinaga T., Higashio K. Identification of heparin-binding stretches of a naturally occurring deleted variant of hepatocyte growth factor (dHGF). Biochim. Biophys. Acta 1998, 1384:93-102.
    • (1998) Biochim. Biophys. Acta , vol.1384 , pp. 93-102
    • Kinosaki, M.1    Yamaguchi, K.2    Murakami, A.3    Ueda, M.4    Morinaga, T.5    Higashio, K.6
  • 20
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon M.A., Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2010, 141:1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 21
    • 0035887033 scopus 로고    scopus 로고
    • Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor
    • Lietha D., Chirgadze D.Y., Mulloy B., Blundell T.L., Gherardi E. Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor. EMBO J. 2001, 20:5543-5555.
    • (2001) EMBO J. , vol.20 , pp. 5543-5555
    • Lietha, D.1    Chirgadze, D.Y.2    Mulloy, B.3    Blundell, T.L.4    Gherardi, E.5
  • 22
    • 0028177817 scopus 로고
    • Mutational analysis and molecular modeling of the N-terminal kringle-containing domain of hepatocyte growth factor identifies amino acid side chains important for interaction with the c-Met receptor
    • Lokker N.A., Presta L.G., Godowski P.J. Mutational analysis and molecular modeling of the N-terminal kringle-containing domain of hepatocyte growth factor identifies amino acid side chains important for interaction with the c-Met receptor. Protein Eng. 1994, 7:895-903.
    • (1994) Protein Eng. , vol.7 , pp. 895-903
    • Lokker, N.A.1    Presta, L.G.2    Godowski, P.J.3
  • 23
    • 0037059771 scopus 로고    scopus 로고
    • The mode of action of heparan and dermatan sulfates in the regulation of hepatocyte growth factor/scatter factor
    • Lyon M., Deakin J.A., Gallagher J.T. The mode of action of heparan and dermatan sulfates in the regulation of hepatocyte growth factor/scatter factor. J. Biol. Chem. 2002, 277:1040-1046.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1040-1046
    • Lyon, M.1    Deakin, J.A.2    Gallagher, J.T.3
  • 24
    • 6344284887 scopus 로고    scopus 로고
    • The interactions of hepatocyte growth factor/scatter factor and its NK1 and NK2 variants with glycosaminoglycans using a modified gel mobility shift assay. Elucidation of the minimal size of binding and activatory oligosaccharides
    • Lyon M., Deakin J.A., Lietha D., Gherardi E., Gallagher J.T. The interactions of hepatocyte growth factor/scatter factor and its NK1 and NK2 variants with glycosaminoglycans using a modified gel mobility shift assay. Elucidation of the minimal size of binding and activatory oligosaccharides. J. Biol. Chem. 2004, 279:43560-43567.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43560-43567
    • Lyon, M.1    Deakin, J.A.2    Lietha, D.3    Gherardi, E.4    Gallagher, J.T.5
  • 25
    • 0029985372 scopus 로고    scopus 로고
    • Emerging multipotent aspects of hepatocyte growth factor
    • Matsumoto K., Nakamura T. Emerging multipotent aspects of hepatocyte growth factor. J. Biochem. 1996, 119:591-600.
    • (1996) J. Biochem. , vol.119 , pp. 591-600
    • Matsumoto, K.1    Nakamura, T.2
  • 27
    • 0028123481 scopus 로고
    • Hairpin loop and second kringle domain are essential sites for heparin binding and biological activity of hepatocyte growth factor
    • Mizuno K., Inoue H., Hagiya M., Shimizu S., Nose T., Shimohigashi Y., Nakamura T. Hairpin loop and second kringle domain are essential sites for heparin binding and biological activity of hepatocyte growth factor. J. Biol. Chem. 1994, 269:1131-1136.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1131-1136
    • Mizuno, K.1    Inoue, H.2    Hagiya, M.3    Shimizu, S.4    Nose, T.5    Shimohigashi, Y.6    Nakamura, T.7
  • 28
    • 18144423534 scopus 로고    scopus 로고
    • Structural basis for fibroblast growth factor receptor activation
    • Mohammadi M., Olsen S.K., Ibrahimi O.A. Structural basis for fibroblast growth factor receptor activation. Cytokine Growth Factor Rev. 2005, 16:107-137.
    • (2005) Cytokine Growth Factor Rev. , vol.16 , pp. 107-137
    • Mohammadi, M.1    Olsen, S.K.2    Ibrahimi, O.A.3
  • 29
    • 0026787652 scopus 로고
    • Functional characterization of human hepatocyte growth factor mutants obtained by deletion of structural domains
    • Okigaki M., Komada M., Uehara Y., Miyazawa K., Kitamura N. Functional characterization of human hepatocyte growth factor mutants obtained by deletion of structural domains. Biochemistry 1992, 31:9555-9561.
    • (1992) Biochemistry , vol.31 , pp. 9555-9561
    • Okigaki, M.1    Komada, M.2    Uehara, Y.3    Miyazawa, K.4    Kitamura, N.5
  • 31
    • 84865139563 scopus 로고    scopus 로고
    • Structural basis for the selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1
    • Parker M.W., Xu P., Li X., Vander Kooi C.W. Structural basis for the selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1. J. Biol. Chem. 2012, 2012:7.
    • (2012) J. Biol. Chem. , vol.2012 , pp. 7
    • Parker, M.W.1    Xu, P.2    Li, X.3    Vander Kooi, C.W.4
  • 32
    • 33847292778 scopus 로고    scopus 로고
    • From Tpr-Met to Met, tumorigenesis and tubes
    • Peschard P., Park M. From Tpr-Met to Met, tumorigenesis and tubes. Oncogene 2007, 26:1276-1285.
    • (2007) Oncogene , vol.26 , pp. 1276-1285
    • Peschard, P.1    Park, M.2
  • 33
    • 0035062394 scopus 로고    scopus 로고
    • The splice variants of vascular endothelial growth factor (VEGF) and their receptors
    • Robinson C.J., Stringer S.E. The splice variants of vascular endothelial growth factor (VEGF) and their receptors. J. Cell Sci. 2001, 114:853-865.
    • (2001) J. Cell Sci. , vol.114 , pp. 853-865
    • Robinson, C.J.1    Stringer, S.E.2
  • 34
    • 0035980123 scopus 로고    scopus 로고
    • Dissociation of heparan sulfate and receptor binding domains of hepatocyte growth factor reveals that heparan sulfate-c-met interaction facilitates signaling
    • Rubin J.S., Day R.M., Breckenridge D., Atabey N., Taylor W.G., Stahl S.J., Wingfield P.T., Kaufman J.D., Schwall R., Bottaro D.P. Dissociation of heparan sulfate and receptor binding domains of hepatocyte growth factor reveals that heparan sulfate-c-met interaction facilitates signaling. J. Biol. Chem. 2001, 276:32977-32983.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32977-32983
    • Rubin, J.S.1    Day, R.M.2    Breckenridge, D.3    Atabey, N.4    Taylor, W.G.5    Stahl, S.J.6    Wingfield, P.T.7    Kaufman, J.D.8    Schwall, R.9    Bottaro, D.P.10
  • 35
    • 0031002920 scopus 로고    scopus 로고
    • Heparin binding and oligomerization of hepatocyte growth factor/scatter factor isoforms. Heparan sulfate glycosaminoglycan requirement for Met binding and signaling
    • Sakata H., Stahl S.J., Taylor W.G., Rosenberg J.M., Sakaguchi K., Wingfield P.T., Rubin J.S. Heparin binding and oligomerization of hepatocyte growth factor/scatter factor isoforms. Heparan sulfate glycosaminoglycan requirement for Met binding and signaling. J. Biol. Chem. 1997, 272:9457-9463.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9457-9463
    • Sakata, H.1    Stahl, S.J.2    Taylor, W.G.3    Rosenberg, J.M.4    Sakaguchi, K.5    Wingfield, P.T.6    Rubin, J.S.7
  • 37
    • 0029897025 scopus 로고    scopus 로고
    • Heparin induces dimerization and confers proliferative activity onto the hepatocyte growth factor antagonists NK1 and NK2
    • Schwall R.H., Chang L.Y., Godowski P.J., Kahn D.W., Hillan K.J., Bauer K.D., Zioncheck T.F. Heparin induces dimerization and confers proliferative activity onto the hepatocyte growth factor antagonists NK1 and NK2. J. Cell Biol. 1996, 133:709-718.
    • (1996) J. Cell Biol. , vol.133 , pp. 709-718
    • Schwall, R.H.1    Chang, L.Y.2    Godowski, P.J.3    Kahn, D.W.4    Hillan, K.J.5    Bauer, K.D.6    Zioncheck, T.F.7
  • 40
    • 3142595278 scopus 로고    scopus 로고
    • Crystal structure of the HGF β-chain in complex with the Sema domain of the Met receptor
    • Stamos J., Lazarus R.A., Yao X., Kirchhofer D., Wiesmann C. Crystal structure of the HGF β-chain in complex with the Sema domain of the Met receptor. EMBO J. 2004, 23:2325-2335.
    • (2004) EMBO J. , vol.23 , pp. 2325-2335
    • Stamos, J.1    Lazarus, R.A.2    Yao, X.3    Kirchhofer, D.4    Wiesmann, C.5
  • 41
    • 0035877708 scopus 로고    scopus 로고
    • Kinase insert domain receptor (KDR) extracellular immunoglobulin-like domains 4-7 contain structural features that block receptor dimerization and vascular endothelial growth factor-induced signaling
    • Tao Q., Backer M.V., Backer J.M., Terman B.I. Kinase insert domain receptor (KDR) extracellular immunoglobulin-like domains 4-7 contain structural features that block receptor dimerization and vascular endothelial growth factor-induced signaling. J. Biol. Chem. 2001, 276:21916-21923.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21916-21923
    • Tao, Q.1    Backer, M.V.2    Backer, J.M.3    Terman, B.I.4
  • 43
    • 0032533765 scopus 로고    scopus 로고
    • Crystal structure of the NK1 fragment of human hepatocyte growth factor at 2.0 A resolution
    • Ultsch M., Lokker N.A., Godowski P.J., de Vos A.M. Crystal structure of the NK1 fragment of human hepatocyte growth factor at 2.0 A resolution. Structure 1998, 6:1383-1393.
    • (1998) Structure , vol.6 , pp. 1383-1393
    • Ultsch, M.1    Lokker, N.A.2    Godowski, P.J.3    de Vos, A.M.4
  • 47
    • 76649105135 scopus 로고    scopus 로고
    • Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling
    • Yang Y., Xie P., Opatowsky Y., Schlessinger J. Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling. Proc. Natl. Acad. Sci. USA 2010, 107:1906-1911.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1906-1911
    • Yang, Y.1    Xie, P.2    Opatowsky, Y.3    Schlessinger, J.4
  • 49


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.